Q92187 (SIA8D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase
EC=2.4.99.-

Alternative name(s):
Alpha-2,8-sialyltransferase 8D
Polysialyltransferase-1
Sialyltransferase 8D
Short name=SIAT8-D
Sialytransferase St8Sia IV
Short name=ST8SiaIV

Gene names

Name:	ST8SIA4
Synonyms:	PST, PST1, SIAT8D

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA), which is present on the embryonic neural cell adhesion molecule (N-CAM), necessary for plasticity of neural cells.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein Potential.
Tissue specificity	Highly expressed in fetal brain, lung and kidney and in adult heart, spleen and thymus. Present to a lesser extent in adult brain, placenta, lung, large and small intestine and peripheral blood leukocytes.
Sequence similarities	Belongs to the glycosyltransferase 29 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	N-glycan processing Inferred from direct assay. Source: BHF-UCL axon guidance Traceable author statement. Source: Reactome ganglioside biosynthetic process Inferred from direct assay. Source: BHF-UCL
Cellular component	integral to Golgi membrane Inferred from electronic annotation. Source: InterPro
Molecular function	alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity Inferred from direct assay. Source: BHF-UCL sialic acid binding Inferred by curator. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase		PRO_0000149293
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 20	13	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	21 – 359	339	Lumenal Potential
Amino acid modifications
	Glycosylation	50	1	N-linked (GlcNAc...) Potential
	Glycosylation	74	1	N-linked (GlcNAc...) Ref.5
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	204	1	N-linked (GlcNAc...) Potential
	Glycosylation	219	1	N-linked (GlcNAc...) Potential
	Glycosylation	327	1	N-linked (GlcNAc...) Potential
	Disulfide bond	142 ↔ 292		Ref.5
	Disulfide bond	156 ↔ 356		Ref.5
Natural variations
	Natural variant	92	1	E → G in a colorectal cancer sample; somatic mutation. Ref.6		VAR_036169

Sequences

	Sequence		Length	Mass (Da)
	Q92187 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: C53FFDF658926D61	FASTA	359	41,295
	10 20 30 40 50 60 MRSIRKRWTI CTISLLLIFY KTKEIARTEE HQETQLIGDG ELSLSRSLVN SSDKIIRKAG 70 80 90 100 110 120 SSIFQHNVEG WKINSSLVLE IRKNILRFLD AERDVSVVKS SFKPGDVIHY VLDRRRTLNI 130 140 150 160 170 180 SHDLHSLLPE VSPMKNRRFK TCAVVGNSGI LLDSECGKEI DSHNFVIRCN LAPVVEFAAD 190 200 210 220 230 240 VGTKSDFITM NPSVVQRAFG GFRNESDREK FVHRLSMLND SVLWIPAFMV KGGEKHVEWV 250 260 270 280 290 300 NALILKNKLK VRTAYPSLRL IHAVRGYWLT NKVPIKRPST GLLMYTLATR FCDEIHLYGF 310 320 330 340 350 WPFPKDLNGK AVKYHYYDDL KYRYFSNASP HRMPLEFKTL NVLHNRGALK LTTGKCVKQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression cloning of a human polysialyltransferase that forms the polysialylated neural cell adhesion molecule present in embryonic brain." Nakayama J., Fukuda M.N., Fredette B., Ranscht B., Fukuda M. Proc. Natl. Acad. Sci. U.S.A. 92:7031-7035(1995) [PubMed: 7624364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity." Angata K., Yen T.Y., El-Battari A., Macher B.A., Fukuda M. J. Biol. Chem. 276:15369-15377(2001) [PubMed: 11279095] [Abstract] Cited for: DISULFIDE BONDS, GLYCOSYLATION AT ASN-74.
[6]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-92.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST8Sia IV

Cross-references

Sequence databases
EMBL GenBank DDBJ	L41680 mRNA. Translation: AAC41775.1. AK292872 mRNA. Translation: BAF85561.1. CH471086 Genomic DNA. Translation: EAW49105.1. BC053657 mRNA. Translation: AAH53657.1.
IPI	IPI00020201.
PIR	I59403.
RefSeq	NP_005659.1. NM_005668.4.
UniGene	Hs.308628.
3D structure databases
ProteinModelPortal	Q92187.
SMR	Q92187. Positions 89-355.
ModBase	Search...
Protein-protein interaction databases
STRING	Q92187.
Protein family/group databases
CAZy	GT29. Glycosyltransferase Family 29.
Polymorphism databases
DMDM	2494834.
Proteomic databases
PRIDE	Q92187.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000231461; ENSP00000231461; ENSG00000113532.
GeneID	7903.
KEGG	hsa:7903.
UCSC	uc003knk.1. human.
Organism-specific databases
CTD	7903.
GeneCards	GC05M100171.
H-InvDB	HIX0005064.
HGNC	HGNC:10871. ST8SIA4.
MIM	602547. gene.
neXtProt	NX_Q92187.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00550000074407.
HOGENOM	HBG717846.
HOVERGEN	HBG056466.
InParanoid	Q92187.
OMA	RSVRKRW.
OrthoDB	EOG4DFPNN.
PhylomeDB	Q92187.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	Q92187.
Bgee	Q92187.
CleanEx	HS_ST8SIA4.
Genevestigator	Q92187.
GermOnline	ENSG00000113532. Homo sapiens.
Family and domain databases
InterPro	IPR001675. Glyco_trans_29. IPR012163. Sialyl_trans. [Graphical view]
KO	K06614.
Pfam	PF00777. Glyco_transf_29. 1 hit. [Graphical view]
PIRSF	PIRSF005557. Sialyl_trans. 1 hit.
ProtoNet	Search...
Other
NextBio	30362.
SOURCE	Search...

Entry information

Entry name

SIA8D_HUMAN

Accession

Primary (citable) accession number: Q92187
Secondary accession number(s): A8KA07, Q92693

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.